Issue 31, 2022

Stereoselective peptide catalysis in complex environments – from river water to cell lysates

Abstract

Many stereoselective peptide catalysts have been established. They consist, like nature's catalysts, of amino acids but have significantly lower molecular weights than enzymes. Whereas enzymes operate with exquisite chemoselectivity in complex biological environments, peptide catalysts are used in pure organic solvents and at higher concentrations. Can a peptide catalyst exhibit chemoselectivity reminiscent of enzymes? Here, we investigated the properties of tripeptide catalysts in complex mixtures in hydrophobic and aqueous solvents. We challenged the catalysts with biomolecules bearing functional groups that could interfere by coordination or reaction with the peptide, the substrates, or intermediates. H-DPro-αMePro-Glu-NHC12H15 emerged through tailoring of the trans/cis ratio of the tertiary amide as a conformationally well-defined tripeptide that catalyzes C–C bond formations with high reactivity and stereoselectivity – regardless of the solvent and compound composition. The chemoselectivity of the tripeptide is so high that it even catalyzes reactions in cell lysates. The findings provoke the question of the potential role of peptide catalysis in nature and during the evolution of enzymes.

Graphical abstract: Stereoselective peptide catalysis in complex environments – from river water to cell lysates

Supplementary files

Article information

Article type
Edge Article
Submitted
10 Apr. 2022
Accepted
27 Maijs 2022
First published
14 Jūn. 2022
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY-NC license

Chem. Sci., 2022,13, 8963-8967

Stereoselective peptide catalysis in complex environments – from river water to cell lysates

T. Schnitzer, J. W. Rackl and H. Wennemers, Chem. Sci., 2022, 13, 8963 DOI: 10.1039/D2SC02044K

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